Characterization of human UDP-glucose dehydrogenase reveals critical catalytic roles for lysine 220 and aspartate 280.

@article{Easley2007CharacterizationOH,
  title={Characterization of human UDP-glucose dehydrogenase reveals critical catalytic roles for lysine 220 and aspartate 280.},
  author={Katherine E Easley and Brandi J Sommer and Gina Boanca and Joseph J. Barycki and Melanie A. Simpson},
  journal={Biochemistry},
  year={2007},
  volume={46 2},
  pages={369-78}
}
Human UDP-glucose dehydrogenase (UGDH) is a homohexameric enzyme that catalyzes two successive oxidations of UDP-glucose to yield UDP-glucuronic acid, an essential precursor for matrix polysaccharide and proteoglycan synthesis. We previously used crystal coordinates for Streptococcus pyogenes UGDH to generate a model of the human enzyme active site. In the studies reported here, we have used this model to identify three putative active site residues: lysine 220, aspartate 280, and lysine 339… CONTINUE READING

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Alteration of the quaternary structure of human UDP-glucose dehydrogenase by a double mutation.

Journal of biochemistry and molecular biology • 2007
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